The Vesicle Associated Membrane Proteins (VAMP) or synaptobrevins are calcium binding proteins. VAMPs, along with synaptosomal associated protein of 25 kDa (SNAP-25) and syntaxin, form the core complex of soluble NSF attachment protein receptor (SNARE) proteins that interact with the soluble proteins N-ethylmaleimide-sensitive factor (NSF) and alpha-SNAP. These membrane associated proteins play a key role in the regulation of vesicle membrane fusion with the plasma membrane. The Clostridium tetani neurotoxin is a metalloprotease with specificity for VAMP. In Alzheimer's disease, VAMP levels of all isoforms appear to be significantly lowered.
Human VAMP-1 is 118 amino acids (aa) in length. It is a type IV transmembrane protein that contains an N-terminal cytoplasmic region (aa 1 - 96) and a 22 aa transmembrane domain (aa 97 - 118). There is one coiled-coil region between aa 33 - 93. Multiple splice variants are known that show two, three, four and 81 aa substitutions for the C-terminal five amino acids. One three aa variant creates a mitochondrial targeting motif. Over aa 1 - 96, human VAMP-1 is 98% aa identical to mouse VAMP-1.
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